scholarly journals Organelle movement and apical accumulation of secretory vesicles in pollen tubes of Arabidopsis thaliana depend on class XI myosins

2020 ◽  
Vol 104 (6) ◽  
pp. 1685-1697
Author(s):  
Xingjuan Wang ◽  
Xiaojing Sheng ◽  
Xiulin Tian ◽  
Yu Zhang ◽  
Yan Li
2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Kazuki Motomura ◽  
Hidenori Takeuchi ◽  
Michitaka Notaguchi ◽  
Haruna Tsuchi ◽  
Atsushi Takeda ◽  
...  

AbstractDuring the double fertilization process, pollen tubes deliver two sperm cells to an ovule containing the female gametes. In the pollen tube, the vegetative nucleus and sperm cells move together to the apical region where the vegetative nucleus is thought to play a crucial role in controlling the direction and growth of the pollen tube. Here, we report the generation of pollen tubes in Arabidopsis thaliana whose vegetative nucleus and sperm cells are isolated and sealed by callose plugs in the basal region due to apical transport defects induced by mutations in the WPP domain-interacting tail-anchored proteins (WITs) and sperm cell-specific expression of a dominant mutant of the CALLOSE SYNTHASE 3 protein. Through pollen-tube guidance assays, we show that the physiologically anuclear mutant pollen tubes maintain the ability to grow and enter ovules. Our findings provide insight into the sperm cell delivery mechanism and illustrate the independence of the tip-localized vegetative nucleus from directional growth control of the pollen tube.


Author(s):  
Cecilia Borassi ◽  
Juliana Pérez Di Giorgio ◽  
María R. Scarpin ◽  
Jorge Muschietti ◽  
José M. Estevez

Cytometry ◽  
1998 ◽  
Vol 32 (4) ◽  
pp. 263-267 ◽  
Author(s):  
A.H.N. de Win ◽  
E.S. Pierson ◽  
C. Timmer ◽  
I.K. Lichtscheidl ◽  
J. Derksen

2001 ◽  
Vol 114 (14) ◽  
pp. 2685-2695 ◽  
Author(s):  
R. M. Parton ◽  
S. Fischer-Parton ◽  
M. K. Watahiki ◽  
A. J. Trewavas

Regulated secretory vesicle delivery, vesicle fusion and rapid membrane recycling are all contentious issues with respect to tip growth in plant, fungal and animal cells. To examine the organisation and dynamics of membrane movements at the growing pollen tube apex and address the question of their relationship to growth, we have used the membrane stain FM4-64 both as a structural marker and as a quantitative assay. Labelling of living Lilium Longiflorum pollen tubes by FM4-64 resulted in a distinct staining pattern in the tube apex, which corresponds spatially to the previously identified cone-shaped `apical clear zone' containing secretory vesicles. Dye uptake could be inhibited by sodium azide and followed a strict temporal sequence from the plasma membrane to a population of small (1-2 μm diameter) discrete internal structures, with subsequent appearance of dye in the apical region and ultimately in vacuolar membranes. Washout of the dye rapidly removed the plasma membrane staining, which was followed by a gradual decline in the apical fluorescence over more than an hour. Injected aqueous FM4-64 solution showed a relatively even distribution within the pollen tube. Association of FM4-64 with apical secretory vesicles was supported by the effects of the inhibitors Brefeldin-A and Cytochalasin-D, which are known to affect the localisation and number of such vesicles, on the FM4-64 staining pattern. Examination of the dynamics of FM4-64 labelling in the pollen tube tip by time-lapse observation, supported by fluorescence-recovery-after-photobleaching (FRAP) analysis, suggested the possibility of distinct pathways of bulk membrane movement both towards and, significantly, away from the apex. Quantitative analysis of FM4-64 distribution in the apex revealed that fluctuations in fluorescence 5 to 10 μm subapically, and to a lesser extent the apical 3 μm, could be related to the periodic oscillation in pollen tube growth rate. This data reveals a quantitative relationship between FM4-64 staining and growth rate within an individual tube.


1981 ◽  
Vol 49 (1) ◽  
pp. 261-272 ◽  
Author(s):  
J.M. Picton ◽  
M.W. Steer

Pollen tubes of Tradescantia were grown in vitro and exposed to 0.3 microgram/ml cytochalasin D for 5 or 10 min. Fine-structural observations revealed no visible effect of the drug on the organelles. Stereological analysis, using a method recently developed by Rose (1980) to obtain sphere size-distributions corrected for section thickness, revealed substantial increase in the number of secretory vesicles present in the cytoplasm around the dictyosomes. Equating the rate of vesicle accumulation with the rate of vesicle production, a total of 5388 vesicles per minute are formed by a growing tube. This corresponds to 2.4 vesicles per minute per dictyosome, and a turnover rate of 3.7 min for a single dictyosome cisterna, or about 15–18.5 min for a complete dictyosome. The calculated vesicle production rate agrees well with that required to sustain the observed growth rate of such tubes, based on the addition of membrane or wall material to the tube tip.


1988 ◽  
Vol 106 (5) ◽  
pp. 1539-1543 ◽  
Author(s):  
T Kohno ◽  
T Shimmen

Pollen tubes show active cytoplasmic streaming. We isolated organelles from pollen tubes and tested their ability to slide along actin bundles in characean cell models. Here, we show that sliding of organelles was ATP-dependent and that motility was lost after N-ethylmaleimide or heat treatment of organelles. On the other hand, cytoplasmic streaming in pollen tube was inhibited by either N-ethylmaleimide or heat treatment. These results strongly indicate that cytoplasmic streaming in pollen tubes is supported by the "actomyosin"-ATP system. The velocity of organelle movement along characean actin bundles was much higher than that of the native streaming in pollen tubes. We suggested that pollen tube "myosin" has a capacity to move at a velocity of the same order of magnitude as that of characean myosin. Moreover, the motility was high at Ca2+ concentrations lower than 0.18 microM (pCa 6.8) but was inhibited at concentration higher than 4.5 microM (pCa 5.4). In conclusion, cytoplasmic streaming in pollen tubes is suggested to be regulated by Ca2+ through "myosin" inactivation.


2012 ◽  
Vol 12 (1) ◽  
pp. 178 ◽  
Author(s):  
Peng Qin ◽  
Dylan Ting ◽  
Andrew Shieh ◽  
Sheila McCormick

2007 ◽  
Vol 64 (3) ◽  
pp. 217-232 ◽  
Author(s):  
Alenka Lovy-Wheeler ◽  
Luis Cárdenas ◽  
Joseph G. Kunkel ◽  
Peter K. Hepler

BIO-PROTOCOL ◽  
2015 ◽  
Vol 5 (12) ◽  
Author(s):  
Marie Dumont ◽  
Arnaud Lehner ◽  
Corinne Loutelier-Bourhis ◽  
Jean-Claude Mollet ◽  
Patrice Lerouge

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Chiara Perico ◽  
Hongbo Gao ◽  
Kate J. Heesom ◽  
Stanley W. Botchway ◽  
Imogen A. Sparkes

AbstractPlant cell organelles are highly mobile and their positioning play key roles in plant growth, development and responses to changing environmental conditions. Movement is acto-myosin dependent. Despite controlling the dynamics of several organelles, myosin and myosin receptors identified so far in Arabidopsis thaliana generally do not localise to the organelles whose movement they control, raising the issue of how specificity is determined. Here we show that a MyoB myosin receptor, MRF7, specifically localises to the Golgi membrane and affects its movement. Myosin XI-K was identified as a putative MRF7 interactor through mass spectrometry analysis. Co-expression of MRF7 and XI-K tail triggers the relocation of XI-K to the Golgi, linking a MyoB/myosin complex to a specific organelle in Arabidopsis. FRET-FLIM confirmed the in vivo interaction between MRF7 and XI-K tail on the Golgi and in the cytosol, suggesting that myosin/myosin receptor complexes perhaps cycle on and off organelle membranes. This work supports a traditional mechanism for organelle movement where myosins bind to receptors and adaptors on the organelle membranes, allowing them to actively move on the actin cytoskeleton, rather than passively in the recently proposed cytoplasmic streaming model.


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